ID G3US35_MELGA Unreviewed; 465 AA.
AC G3US35;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 2.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Aldehyde dehydrogenase {ECO:0000256|PIRNR:PIRNR036492};
OS Meleagris gallopavo (Wild turkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Meleagridinae; Meleagris.
OX NCBI_TaxID=9103 {ECO:0000313|Ensembl:ENSMGAP00000018504.2, ECO:0000313|Proteomes:UP000001645};
RN [1] {ECO:0000313|Ensembl:ENSMGAP00000018504.2, ECO:0000313|Proteomes:UP000001645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20838655; DOI=10.1371/journal.pbio.1000475;
RA Dalloul R.A., Long J.A., Zimin A.V., Aslam L., Beal K., Blomberg L.A.,
RA Bouffard P., Burt D.W., Crasta O., Crooijmans R.P., Cooper K.,
RA Coulombe R.A., De S., Delany M.E., Dodgson J.B., Dong J.J., Evans C.,
RA Frederickson K.M., Flicek P., Florea L., Folkerts O., Groenen M.A.,
RA Harkins T.T., Herrero J., Hoffmann S., Megens H.J., Jiang A., de Jong P.,
RA Kaiser P., Kim H., Kim K.W., Kim S., Langenberger D., Lee M.K., Lee T.,
RA Mane S., Marcais G., Marz M., McElroy A.P., Modise T., Nefedov M.,
RA Notredame C., Paton I.R., Payne W.S., Pertea G., Prickett D., Puiu D.,
RA Qioa D., Raineri E., Ruffier M., Salzberg S.L., Schatz M.C., Scheuring C.,
RA Schmidt C.J., Schroeder S., Searle S.M., Smith E.J., Smith J.,
RA Sonstegard T.S., Stadler P.F., Tafer H., Tu Z.J., Van Tassell C.P.,
RA Vilella A.J., Williams K.P., Yorke J.A., Zhang L., Zhang H.B., Zhang X.,
RA Zhang Y., Reed K.M.;
RT "Multi-platform next-generation sequencing of the domestic turkey
RT (Meleagris gallopavo): genome assembly and analysis.";
RL PLoS Biol. 8:E1000475-E1000475(2010).
RN [2] {ECO:0000313|Ensembl:ENSMGAP00000018504.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-hexadecenal + H2O + NAD(+) = (E)-hexadec-2-enoate + 2
CC H(+) + NADH; Xref=Rhea:RHEA:36135, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17585, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:72745;
CC Evidence={ECO:0000256|ARBA:ARBA00035777};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesal + H2O + NAD(+) = (2E,6E)-farnesoate + 2 H(+)
CC + NADH; Xref=Rhea:RHEA:24216, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15894, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:83276; EC=1.2.1.94;
CC Evidence={ECO:0000256|ARBA:ARBA00036228};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + hexadecanoate + NADH = H2O + hexadecanal + NAD(+);
CC Xref=Rhea:RHEA:33739, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17600, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; Evidence={ECO:0000256|ARBA:ARBA00035953};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2,6,10,14-tetramethylpentadecanal + H2O + NAD(+) = 2,6,10,14-
CC tetramethylpentadecanoate + 2 H(+) + NADH; Xref=Rhea:RHEA:44016,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:49189,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:77268;
CC Evidence={ECO:0000256|ARBA:ARBA00035974};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=22-oxodocosanoate + H2O + NAD(+) = docosanedioate + 2 H(+) +
CC NADH; Xref=Rhea:RHEA:39015, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:76298,
CC ChEBI:CHEBI:76299; Evidence={ECO:0000256|ARBA:ARBA00036932};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) + octadecanal = 2 H(+) + NADH + octadecanoate;
CC Xref=Rhea:RHEA:44020, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17034, ChEBI:CHEBI:25629, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; Evidence={ECO:0000256|ARBA:ARBA00035984};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) + octanal = 2 H(+) + NADH + octanoate;
CC Xref=Rhea:RHEA:44100, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17935, ChEBI:CHEBI:25646, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; Evidence={ECO:0000256|ARBA:ARBA00000589};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) + tetradecanal = 2 H(+) + NADH + tetradecanoate;
CC Xref=Rhea:RHEA:44172, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30807, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:84067; Evidence={ECO:0000256|ARBA:ARBA00035786};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + heptanal + NAD(+) = 2 H(+) + heptanoate + NADH;
CC Xref=Rhea:RHEA:44108, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32362, ChEBI:CHEBI:34787, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; Evidence={ECO:0000256|ARBA:ARBA00036881};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a fatty aldehyde + H2O + NAD(+) = a fatty acid + 2 H(+) +
CC NADH; Xref=Rhea:RHEA:49832, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:35746, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; Evidence={ECO:0000256|ARBA:ARBA00036717};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.3;
CC Evidence={ECO:0000256|ARBA:ARBA00024149};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=decanal + H2O + NAD(+) = decanoate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:44104, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:27689, ChEBI:CHEBI:31457, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; Evidence={ECO:0000256|ARBA:ARBA00036332};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanoate + 2 H(+) + NADH = dodecanal + H2O + NAD(+);
CC Xref=Rhea:RHEA:44168, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:18262, ChEBI:CHEBI:27836, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; Evidence={ECO:0000256|ARBA:ARBA00036265};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004131}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004131}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004131}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|PIRNR:PIRNR036492,
CC ECO:0000256|RuleBase:RU003345}.
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DR AlphaFoldDB; G3US35; -.
DR Ensembl; ENSMGAT00000019899.2; ENSMGAP00000018504.2; ENSMGAG00000006870.3.
DR GeneTree; ENSGT00940000157944; -.
DR HOGENOM; CLU_005391_3_1_1; -.
DR InParanoid; G3US35; -.
DR Proteomes; UP000001645; Chromosome 21.
DR Bgee; ENSMGAG00000006870; Expressed in duodenum and 17 other cell types or tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0006081; P:cellular aldehyde metabolic process; IEA:InterPro.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR012394; Aldehyde_DH_NAD(P).
DR PANTHER; PTHR43570; ALDEHYDE DEHYDROGENASE; 1.
DR PANTHER; PTHR43570:SF9; ALDEHYDE DEHYDROGENASE FAMILY 3 MEMBER A2; 1.
DR Pfam; PF00171; Aldedh; 1.
DR PIRSF; PIRSF036492; ALDH; 2.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Microsome {ECO:0000256|ARBA:ARBA00022848};
KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR036492,
KW ECO:0000256|RuleBase:RU003345};
KW Reference proteome {ECO:0000313|Proteomes:UP000001645};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 439..463
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 102..397
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT COILED 23..50
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 182
FT /evidence="ECO:0000256|PIRSR:PIRSR036492-1,
FT ECO:0000256|PROSITE-ProRule:PRU10007"
FT ACT_SITE 216
FT /evidence="ECO:0000256|PIRSR:PIRSR036492-1"
SQ SEQUENCE 465 AA; 50814 MW; E9AB3E7449BAE32B CRC64;
MGRMAEVVGR ARAAFSSGRS RPLEFRLQQL KNLERMVQEK EREILAAIGA DLHKCGRNAY
SHEIMGGAGG SVRQPRAAGG GPASLMGVCV GAREEHEGCV CLLGNAVVVK PSEISEHTSQ
LIANILPQYL DPELYPVVTG GVPETTELLT QRFDHILYTG NSAVGKIVMA AAAKHLTPVT
LELGGKSPCY IDTDCDLAIA CRRITWGKYM NCGQTCIAPD YILCHPSIQS QVVENIKATL
QEFYGEDVKK CPDYERIINK RHFKRITSLL EGQKIAHGGE TDEASCFIAP TILTDVSAES
KVMEEEIFGP VLPIVSVKNV DEAIEFINRR EKPLALYVFS NDKKLIKRVI SETSSGGVTG
NDVIMHFFLS TLPFGGVGNS GMGAYHGKHS FDTFSHHRSC LIKDLKMEGT NTVRYPPSSQ
KKLDWAKFFI LKRFNKGRLG LIMLALLGVV AAVVIKVSCG SLLST
//
